Electron paramagnetic resonance spectroscopy of the heme domain of inducible nitric oxide synthase: Binding of ligands at the arginine site induces changes in the heme ligation geometry

Biochemistry

Volumn 35, Issue 24, 1996, Pages 7626-7630

  Salerno, John C ^a   Martasek, Pavel ^b   Roman, Linda J ^b   Masters, Bettie Sue S ^b  

^a RENSSELAER POLYTECHNIC INSTITUTE   (United States)

^b UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE DERIVATIVE; HEMATIN; HEME; LIGAND; N(G) HYDROXYARGININE; N(G) METHYLARGININE; N(G) NITROARGININE; NITRIC OXIDE SYNTHASE;

ARTICLE; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; GEOMETRY; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL;

ANIMALS; ARGININE; BASE SEQUENCE; BINDING SITES; CLONING, MOLECULAR; DNA PRIMERS; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEME; ISOENZYMES; LIGANDS; MICE; MOLECULAR SEQUENCE DATA; NITRIC OXIDE SYNTHASE; POLYMERASE CHAIN REACTION; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; RECOMBINANT PROTEINS;

ESCHERICHIA COLI;

EID: 0029892990     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi960607l     Document Type: Article

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